IsdA Protects Staphylococcus aureus against the Bactericidal Protease Activity of Apolactoferrin
作者： Simon R. Clarke , Simon J. Foster
DOI: 10.1128/IAI.01530-07
关键词: Staphylococcus aureus 、 Protease inhibitor (biology) 、 Microbiology 、 Enzyme 、 Antimicrobial peptides 、 Lactoferrin 、 Protease 、 Recombinant DNA 、 Biology 、 Escherichia coli
摘要: An important facet of the Staphylococcus aureus host-pathogen interaction is ability invading bacterium to evade host innate defenses, particularly cocktail antimicrobial peptides. In this work, we showed that IsdA, a surface protein S. which required for nasal colonization, binds lactoferrin, most abundant antistaphylococcal polypeptide in human secretions. The presence IsdA on confers resistance killing by lactoferrin. addition, bactericidal activity lactoferrin was inhibited addition phenylmethylsulfonyl fluoride, implicating serine protease aureus. Recombinant competitive inhibitor activity. Reciprocally, antibody reactive enhanced Thus, can protect against and acts as inhibitor.
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